Perini, L., Gostinčar, C., Gunde -Cimerman, N., 2019. Fungal and bacterial diversity of Svalbard subglacial ice. Scientific Reports 9, 20230.

https://doi.org/10.1038/s41598-019-56290-5 The composition of fungal and bacterial communities in three polythermal glaciers and associated aquatic environments in Kongsfjorden, Svalbard was analysed using a combination of cultivation and amplicon sequencing. 109 fungal strains belonging to 30 mostly basidiomycetous species were isolated from glacial 3 Glaciozyma Phenoliferia psychrophenolica samples with counts up to 10 CFU/100 ml. -related taxon and were the dominant species. Unexpectedly, amplicon sequencing uncovered sequences of Chytridiomycota in all Malassezia restricta samples and Rozellomycota in sea water, lake water, and tap water. Sequences of and of Hortaea werneckii the extremely halotolerant were also found in subglacial habitats for the first time. Overall, the fungal communities within a glacier and among glaciers were diverse and spatially heterogenous. Contrary Flavobacterium to this, there was a large overlap between the bacterial communities of different glaciers, with sp. being the most frequently isolated. In amplicon sequencing Actinobacteria and Proteobacteria sequences were the most abundant.

Petrone, P., Pucci, P., Niola, M., Baxter, P.J., Fontanarosa, C., Giordano, G., Graziano, V., Sirano, F., Amoresano, A., 2020. Heat-induced brain vitrification from the Vesuvius eruption in c.e. 79. New England Journal of Medicine 382, 383-384.

https://www.nejm.org/doi/10.1056/NEJMc1909867 Correspondence: The rapid rise in extreme heat during the Vesuvius eruption in c.e. 79 resulted in the conversion of human tissue to glass (vitrification). Among the recent finds at Herculaneum was tissue residue that could be identified by chemical methods as vitrified brain tissue.

Petzold, A., Lu, C.- H., Groves, M., Gobom, J., Zetterberg, H., Shaw, G., O'Connor, S., 2020. Protein aggregate formation permits millennium-old brain preservation. Journal of The Royal Society Interface 17, 20190775. https://doi.org/10.1098/rsif.2019. 0775

Human proteins have not been reported to survive in free nature, at ambient temperature, for long periods. Particularly, the human brain rapidly dissolves after death due to auto-proteolysis and putrefaction. The here presented discovery of 2600-year-old brain proteins from a radiocarbon dated human brain provides new evidence for extraordinary long-term stability of non-amyloid protein aggregates. Immunoelectron microscopy confirmed the preservation of neurocytoarchitecture in the ancient brain, which appeared shrunken and compact compared to a modern brain. Resolution of intermediate filaments (IFs) from protein aggregates took 2 - 12 months. Immunoassays on micro-dissected brain tissue homogenates revealed the preservation of the known protein topography for grey and white matter for type III (glial fibrillary acidic protein, GFAP) and IV (neurofilaments, Nfs) IFs. Mass spectrometry data could be matched to a number of peptide sequences, notably for GFAP and Nfs. Preserved immunogenicity of the prehistoric human brain proteins was demonstrated by antibody generation (GFAP, Nfs, myelin basic protein). Unlike brain proteins, DNA was of poor quality preventing reliable sequencing. These long-term data from a unique ancient human brain demonstrate that aggregate formation permits for the preservation of brain proteins for millennia.

Pfeiffer, D., Schüler, D., 2020. Quantifying the benefit of a dedicated 'magnetoskeleton' in bacterial magnetotaxis by live-cell motility tracking and soft agar swimming assay. Applied and Environmental Microbiology 86, e01976-19.

http://aem.asm.org/content/86/3/e01976-19.abstract Abstract: The alphaproteobacterium Magnetospirillum gryphiswaldense has the intriguing ability to navigate within magnetic fields, a behavior named magnetotaxis, governed by the formation of magnetosomes,